LMBD1_XENTR
ID LMBD1_XENTR Reviewed; 539 AA.
AC Q0VGV9;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Lysosomal cobalamin transport escort protein LMBD1 {ECO:0000250|UniProtKB:Q9NUN5};
DE Short=LMBD1;
DE AltName: Full=LMBR1 domain-containing protein 1;
GN Name=lmbrd1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lysosomal membrane chaperone required to export cobalamin
CC (vitamin B12) from the lysosome to the cytosol, allowing its conversion
CC to cofactors. Targets ABCD4 transporter from the endoplasmic reticulum
CC to the lysosome. Then forms a complex with lysosomal ABCD4 and
CC cytoplasmic MMACHC to transport cobalamin across the lysosomal membrane
CC (By similarity). May play a role in mediating and regulating the
CC internalization of the insulin receptor (By similarity).
CC {ECO:0000250|UniProtKB:Q8K0B2, ECO:0000250|UniProtKB:Q9NUN5}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NUN5}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q9NUN5}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q8K0B2}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the LIMR family. LMBRD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC080477; AAH80477.1; -; mRNA.
DR RefSeq; NP_001072184.1; NM_001078716.1.
DR AlphaFoldDB; Q0VGV9; -.
DR SMR; Q0VGV9; -.
DR STRING; 8364.ENSXETP00000062645; -.
DR PaxDb; Q0VGV9; -.
DR GeneID; 779630; -.
DR KEGG; xtr:779630; -.
DR CTD; 55788; -.
DR Xenbase; XB-GENE-1015707; lmbrd1.
DR eggNOG; ENOG502QQ2T; Eukaryota.
DR InParanoid; Q0VGV9; -.
DR OrthoDB; 744771at2759; -.
DR Reactome; R-XTR-9758881; Uptake of dietary cobalamins into enterocytes.
DR Reactome; R-XTR-9758890; Transport of RCbl within the body.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000011753; Expressed in mesonephros and 12 other tissues.
DR ExpressionAtlas; Q0VGV9; baseline.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0038016; P:insulin receptor internalization; ISS:UniProtKB.
DR GO; GO:0061462; P:protein localization to lysosome; ISS:UniProtKB.
DR GO; GO:0072665; P:protein localization to vacuole; IBA:GO_Central.
DR InterPro; IPR006876; LMBR1-like_membr_prot.
DR Pfam; PF04791; LMBR1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cobalamin; Cobalt; Endoplasmic reticulum; Glycoprotein;
KW Lysosome; Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..539
FT /note="Lysosomal cobalamin transport escort protein LMBD1"
FT /id="PRO_0000365820"
FT TOPO_DOM 1..7
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..98
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..362
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..484
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..539
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 539 AA; 61556 MW; 297F320713E449EA CRC64;
MATGSTELLI GWCIFGVLLL AILAFCWVYV RKYQSHQESE VISTITAISS LAIALITSAL
LPVDIFLVSF MKNHNGTFKD WAESNTTRLQ IENTVLIGYY TLYSIILFCV FLWIPFVYFY
YEEKDDTDGS QCSQIANAFK YTSGFILVCS CLLLIGAFAP LDIHTNKNST DLDKIKLLFL
ELGSSNGLAA LSFSISSLTL IGMLAAITYT AYGMSALPLN LIKGTRNAHY ERLENSEDIE
EVEQQVERIM SKCKDGRPLS SKDRQALYKL KEKLRTLKRR DRHLEYHENN CWTKCCIVIR
PFKIIWGILF ILVALLFIVS LFLSNLDKAL HSAGIDSGFI IFGTNLTNPL NMLLPVLQTV
FPLDYIFITI ITMYFIFTSM AGIRNMGIWF FWIRLYKIRR RRTRPQALLF LCMILLLIVL
HTSYMIYSLA PQYVMYGSQK YLWENNSTQE TAIGNSSASV LKDCDASAPE DQCTVTRTYL
FLHKFWFFSS IYYFGNWAFI VVFVIGLIVS CCKGKKSVIE GEVEDDDSDL SDDEEHPYA
